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Chen Rongzhong,Yang Feng,Xu Xun. 2000. Purification, characterization and ELISA of metallothionein from red scorponifish, Sebastiscus marmoratus. Acta Oceanologica Sinica, (1):137－144

Purification, characterization and ELISA of metallothionein from red scorponifish, Sebastiscus marmoratus

Received:January 15, 1999 Revised:April 18, 1999

DOI：

Key words:Red scorponilish metallothionein purification immunoassay

中文关键词: Red scorponilish metallothionein purification immunoassay

基金项目:

Author Name	Affiliation
Chen Rongzhong	Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China
Yang Feng	Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China
Xu Xun	Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, China

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Abstract:

Metallothionein(MT) is a low molecular weight (MW)and heatstable metal-binding prorein.It has been proved that the synthesis of MT in marine animals can be induced by various heavy metals at genetic level.Consequently, high level of MT can be used as sign of heavy metal pollution.
In this article, red scorponifish MT was purified by Sephadex G-75 gel filtration and DEAE-Sepharose CL-6B ion exchange chromatography.The results of amino acids composition analysis showed that the protein contains 35%cysteine (Cys),but no aromatic residues.MW was ahout 6.7 kD, and pI is 4.0 and 4.2,respectively.The antibody was raised in white rabbits by injection by MT conjugated with BSA, and then purified on Protein A beads and labeled with horseradish peroxidase.Quantification of MT by ELISA indicated that the concentration of MT from induced and noninduced fish liver extraction were 450 and 20 μg/cm³,respectively.

中文摘要:

Metallothionein(MT) is a low molecular weight (MW)and heatstable metal-binding prorein.It has been proved that the synthesis of MT in marine animals can be induced by various heavy metals at genetic level.Consequently, high level of MT can be used as sign of heavy metal pollution.
In this article, red scorponifish MT was purified by Sephadex G-75 gel filtration and DEAE-Sepharose CL-6B ion exchange chromatography.The results of amino acids composition analysis showed that the protein contains 35%cysteine (Cys),but no aromatic residues.MW was ahout 6.7 kD, and pl is 4.0 and 4.2,respectively.The antibody was raised in white rabbits by injection by MT conjugated with BSA, and then purified on Protein A beads and labeled with horseradish peroxidase.Quantification of MT by ELISA indicated that the concentration of MT from induced and noninduced fish liver extraction were 450 and 20 μg/cm³,respectively.

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